SCP25_ARATH
ID SCP25_ARATH Reviewed; 473 AA.
AC Q8L9Y0; Q9SGA9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine carboxypeptidase-like 25;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL25; OrderedLocusNames=At3g02110; ORFNames=F1C9.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=15908604; DOI=10.1104/pp.104.057950;
RA Fraser C.M., Rider L.W., Chapple C.;
RT "An expression and bioinformatics analysis of the Arabidopsis serine
RT carboxypeptidase-like gene family.";
RL Plant Physiol. 138:1136-1148(2005).
CC -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65698.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC011664; AAF14826.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73764.1; -; Genomic_DNA.
DR EMBL; AY037210; AAK59795.1; -; mRNA.
DR EMBL; BT002657; AAO11573.1; -; mRNA.
DR EMBL; AY088154; AAM65698.1; ALT_INIT; mRNA.
DR RefSeq; NP_186860.1; NM_111077.4.
DR AlphaFoldDB; Q8L9Y0; -.
DR SMR; Q8L9Y0; -.
DR STRING; 3702.AT3G02110.1; -.
DR ESTHER; arath-SCP25; Carboxypeptidase_S10.
DR MEROPS; S10.A40; -.
DR PaxDb; Q8L9Y0; -.
DR PRIDE; Q8L9Y0; -.
DR ProteomicsDB; 232919; -.
DR EnsemblPlants; AT3G02110.1; AT3G02110.1; AT3G02110.
DR GeneID; 821207; -.
DR Gramene; AT3G02110.1; AT3G02110.1; AT3G02110.
DR KEGG; ath:AT3G02110; -.
DR Araport; AT3G02110; -.
DR TAIR; locus:2078598; AT3G02110.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_0_1; -.
DR InParanoid; Q8L9Y0; -.
DR OMA; KFSWNTV; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q8L9Y0; -.
DR PRO; PR:Q8L9Y0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L9Y0; baseline and differential.
DR Genevisible; Q8L9Y0; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..473
FT /note="Serine carboxypeptidase-like 25"
FT /id="PRO_0000274640"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
FT ACT_SITE 395
FT /evidence="ECO:0000250"
FT ACT_SITE 447
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..358
FT /evidence="ECO:0000250"
FT DISULFID 252..263
FT /evidence="ECO:0000250"
FT DISULFID 288..326
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 53401 MW; 3E0FB3AEE4CE47BC CRC64;
MAMAKLAIFT TLMAILVMTS QGRIPTEGGE KEAEADRITS LPGQPNVTFE QFSGYVTVDK
LSGRSLFYWL TEASDLPLSK PLVIWLNGGP GCSSVAYGAS EEIGPFRISK GGSGLYLNKF
AWNSISNLLF LEAPAGVGFS YTNRSSDLFN TGDRRTAKDS LQFLIQWLHR FPRYNHREIY
ITGESYAGHY VPQLAKEIMN YNKRSKNPLN LKGIMVGNAV TDNHYDNLGT VSYWWSHAMI
SDRTYHQLIS TCDFSRQKES DECETLYSYA MEQEFGNIDQ YNIYAPPCNK SSDGGGSYNG
SSGRRSMRLP HLPHSVLRKI SGYDPCTERY AEIYYNRPDV QKALHANTTK IPYKWTACSE
VLNRNWNDTD STVLPIYREM IAGGIRVWVF SGDVDSVVPV TATRYSLARL SLSTKLPWYP
WYVKKQVGGW TEVYEGLTFV TVRGAGHEVP LFKPRAAFEL FKYFLRGKPL PKA
